In collaboration with the Molecular Targets Development Program, CCR, we have reported the solution structure of the novel anti-viral protein Scytovirin, published in the Journal of Molecular Biology. Our studies included examination of the oligosaccharide binding, which is the key element of the entry-inhibition mechanism proposed for Scytovirin. This protein exhibits remarkable anti-viral activity against HIV and Ebola. Animal studies are underway to guide future development and will be combined with structurally guided engineering studies. We are continuing to study the details of the oligosaccharide binding. Through the use of site engineering, we hope to generate a protein with only one active binding site, that would facilitate both a detailed structural analyses and be valuable in dissecting the interaction with viral gp41 and gp120.